Demonstration of Cu-Zn superoxide dismutase in rat liver peroxisomes. Biochemical and immunochemical evidence.

نویسندگان

  • G S Dhaunsi
  • S Gulati
  • A K Singh
  • J K Orak
  • K Asayama
  • I Singh
چکیده

In this study, by using highly purified rat liver peroxisomes, we provide evidence from analytical cell fractionation, Western blot, and immunocytochemical analysis that Cu-Zn superoxide dismutase is present in animal peroxisomes. Treatment with ciprofibrate, a peroxisome proliferator, increased the peroxisomal superoxide dismutase activity by 3-fold with no effect on mitochondrial activity but a marked decrease in cytosolic superoxide dismutase activity, further supporting that besides cytosolic and mitochondrial localization, Cu-Zn superoxide dismutase is present in peroxisomes also. Demonstration of superoxide dismutase in peroxisomes suggests a new role for this organelle in pathophysiological conditions, such as ischemia-reperfusion injury.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Peroxisomes as a source of superoxide and hydrogen peroxide in stressed plants.

Superoxide dismutases (SODs) and superoxide radicals in peroxisomes Peroxisomes are subcellular respiratory organelles that contain catalase and H202-producing flavin oxidases as basic enzymatic constituents [1,2]. In recent years, it has become increasingly clear that peroxisomes carry out essential functions in almost all eukaryotic cells [3-51, and an important characteristic of peroxisomes ...

متن کامل

Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells.

The intracellular localization of Cu,Zn superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1) has been examined by immunofluorescence using four monoclonal anti-Cu,Zn superoxide dismutase antibodies raised against a recombinant human Cu,Zn superoxide dismutase derivative produced and purified from Escherichia coli. Colocalization with catalase, a peroxisomal matrix enzyme, wa...

متن کامل

Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase.

The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2*-) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither sca...

متن کامل

Peroxisomal copper, zinc superoxide dismutase. Characterization of the isoenzyme from watermelon cotyledons.

The biochemical and immunochemical characterization of a superoxide dismutase (SOD, EC 1.15.1.1) from peroxisomal origin has been carried out. The enzyme is a Cu,Zn-containing SOD (CuZn-SOD) located in the matrix of peroxisomes from watermelon (Citrullus vulgaris Schrad.) cotyledons (L.M. Sandalio and L.A. del Río [1988] Plant Physiol 88: 1215-1218). The amino acid composition of the enzyme was...

متن کامل

Increased levels of peroxisomal active oxygen-related enzymes in copper-tolerant pea plants.

The effect in vivo of high nutrient levels of copper (240 micromolar) on the activity of different metalloenzymes containing Cu, Mn, Fe, and Zn, distributed in chloroplasts, peroxisomes, and mitochondria, was studied in leaves of two varieties of Pisum sativum L. plants with different sensitivity to copper. The metalloenzymes studied were: cytochrome c oxidase, Mn-superoxide dismutase (Mn-SOD) ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 267 10  شماره 

صفحات  -

تاریخ انتشار 1992